Photooxidase system of Rhodospirillum rubrum III. The role of rhodoquinone and ubiquinone in the activity of preparations of chromatophores and photoreaction centers.
The role of rhodoquinone and ubiquinone in the oxygen photoreducing (photooxidase) activity of Rhodospirillum rubrum was investigated. The sole addition of purified rhodoquinone restored photooxidase activity in isolated chromatophores which had been extracted with organic solvents and which were apparently free of secondary acceptor ubiquinone. Rhodoquinone also enhanced photooxidase activity in photoreaction center preparations from which secondary ubiquinone seemed to have been removed. Those results suggest that rhodoquinone accepts electrons directly from primary ubiquinone during chromatophore photooxidase activity. In contrast, rhodoquinone does not participate in the basal activity of photoreaction center preparations, which seems to result from the autooxidation of both primary and secondary ubiquinone.
D020130:Bacterial Chromatophores / Q000201:enzymology*; D001426:Bacterial Proteins; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010084:Oxidation-Reduction; D010777:Photochemistry; D011808:Quinone Reductases / Q000378:metabolism*; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D014451:Ubiquinone / Q000031:analogs & derivatives* / Q000378:metabolism*
D001426:Bacterial Proteins; D014451:Ubiquinone; D009247:NADH, NADPH Oxidoreductases; D011808:Quinone Reductases; C033839:photooxidase, Rhodospirillum rubrum; C003304:rhodoquinone